Abstract:
:For influenza H5N1 hemagglutinin, a switch from SA-alpha-2, 3-Gal to SA-alpha-2, 6-Gal receptor specificity is a critical step leading to the conversion from avian-to-human to human-to-human infection. Therefore, the understanding of the binding modes of SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal to H5N1 hemagglutinin will be very important for the examination of possible mutations needed for going from an avian to a human flu virus. Based on the available H5N1 hemagglutinin crystal structure, the binding profiles between H5N1 hemagglutinin and two saccharide ligands, SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal, were investigated by ab initio quantum mechanics, molecular docking, molecular mechanics, and molecular dynamics simulations. It was found that SA-alpha-2, 3-Gal has strong multiple hydrophobic and hydrogen bond interactions in its trans conformation with H5N1 hemagglutinin, whereas the SA-alpha-2, 6-Gal only shows weak interactions in a different conformation (cis type).
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Li M,Wang Bdoi
10.1016/j.bbrc.2006.06.179subject
Has Abstractpub_date
2006-09-01 00:00:00pages
662-8issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)01431-8journal_volume
347pub_type
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